Research workbench
Crystal structure of the MYOSTATIN:FOLLISTATIN 288 complex
Analyse Crystal structure of the MYOSTATIN:FOLLISTATIN 288 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HH2
- Type
- protein
- Length
- 771 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GROWTH/DIFFERENTIATION factor 8; Follistatin
- UniProt
- O08689, P19883
- Ligands
- PO4
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GROWTH/DIFFERENTIATION factor 8 | protein | 109 | 12% helix, 44% strand | O08689 |
| C | Follistatin | protein | 278 | 18% helix, 27% strand | P19883 |
| D | Follistatin | protein | 275 | 18% helix, 28% strand | P19883 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, D, B, C
- CIT · Citric acid · additive · 2 copies · chains B, C, A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 814 | 0.74 | 0.79 | 88 | CIT |
| 2 | 628 | 0.70 | 0.78 | 64 | PO4 |
| 3 | 678 | 0.67 | 0.76 | 77 | empty |
| 4 | 661 | 0.67 | 0.76 | 73 | empty |
| 5 | 238 | 0.63 | 0.82 | 33 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1570 Ų buried · 26 hydrogen bonds · protein-protein
- A–D · 1529 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1235 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 673 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 419 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 45 disulfide (disulfide).
Compared structures
- 3HH2 · Crystal structure of the myostatin:follistatin 288 complex · the same entry in another collection · chain D against D, TM-score 1.00
- P19883 · AlphaFold monomer V2.0 prediction for follistatin (P19883) · a predicted model of the same protein · chain C against A, TM-score 0.98
- O08689 · AlphaFold monomer V2.0 prediction for GROWTH/DIFFERENTIATION factor 8 (O08689) · a predicted model of the same protein · chain A against A, TM-score 0.75
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O08689
- Every structure of UniProt P19883
- Elsewhere: RCSB PDB 3HH2 · PDBe 3HH2 · UniProt O08689 · UniProt P19883
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